Recombinant Human Purine Nucleoside Phosphorylase (PNP) Protein (His-SUMO)

Name: Recombinant Human Purine Nucleoside Phosphorylase (PNP) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-09880P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Purine Nucleoside Phosphorylase (PNP) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P00491
Target Symbol	PNP
Synonyms	FLJ94043; FLJ97288; FLJ97312; Inosine phosphorylase; Inosine-guanosine phosphorylase; MGC117396; MGC125915; MGC125916; NP; Np1; Nucleoside phosphorylase; PNP; Pnp1; PNPH_HUMAN; PRO1837; PUNP; Purine nucleoside orthophosphate ribosyltransferase; Purine nucleoside phosphorylase 5a; Purine nucleoside phosphorylase
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MENGYTYEDYKNTAEWLLSHTKHRPQVAIICGSGLGGLTDKLTQAQIFDYGEIPNFPRSTVPGHAGRLVFGFLNGRACVMMQGRFHMYEGYPLWKVTFPVRVFHLLGVDTLVVTNAAGGLNPKFEVGDIMLIRDHINLPGFSGQNPLRGPNDERFGDRFPAMSDAYDRTMRQRALSTWKQMGEQRELQEGTYVMVAGPSFETVAECRVLQKLGADAVGMSTVPEVIVARHCGLRVFGFSLITNKVIMDYESLEKANHEEVLAAGKQAAQKLEQFVSILMASIPLPDKAS
Expression Range	1-289aa
Protein Length	Full Length
Mol. Weight	48.1kDa
Research Area	Metabolism
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Catalyzes the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. Preferentially acts on 6-oxopurine nucleosides including inosine and guanosine.
Subcellular Location	Cytoplasm.
Protein Families	PNP/MTAP phosphorylase family
Database References	HGNC: 7892 OMIM: 164050 KEGG: hsa:4860 STRING: 9606.ENSP00000354532 UniGene: PMID: 29915028 The PNP rs1049564 T allele is a loss-of-function variant that induces S-phase block and IFN pathway activation in lymphocytes. The S-phase block could be rescued in our in vitro experiments, suggesting the potential for personalized treatment. PMID: 28859258 Data show that the mutations in purine nucleoside phosphorylase (PNP) alters the enthalpy-entropy balance with little effect on the catalytic rates. PMID: 27976868 Data (including data from empirical valence bond/molecular dynamic simulations) suggest that PNP substrate specificity for inosine and guanosine is a direct result of electrostatic preorganization energy along the reaction coordinate. PMID: 26985580 the binding mechanism of a transition state analogue (DADMe-immucillin-H) to the purine nucleoside phosphorylase (PNP) enzyme, is reported. PMID: 25625196 Data show that [15N, 2H]His8-purine nucleoside phosphorylase (PNP) had reduced catalytic site chemistry larger than proportional to the enzymatic mass difference. PMID: 26305965 Study of genetic heterogeneity in systemic lupus erythematosus, the top associations in European ancestry were protein kinase, cyclic GMP-dependent, type I (PRKG1) rs7897633 (P(Meta) = 2.75 x 10(-8)) and purine nucleoside phosphorylase (PNP) rs1049564 (P(Meta) = 1.24 x 10(-7)). PMID: 25338677 Human small intestine is a key site for ribavirin phosphorolysis and that PNP is primarily involved in the metabolism. PMID: 24107682 insufficient data to evaluated impact of genetic polymorphisms on disease susceptibility PMID: 24792412 Complete lack of PNP triggers accumulation of deoxyguanosine, thereby disrupting B-cell development, the consequence of which is more profound with time, as was found in the older sister. PMID: 22578971 Biochemical and genetic data on a cohort of seven patients from six families identified as PNPase deficient, is reported. PMID: 22132981 This study for the first time describes elevated levels of alpha synuclein in pancreatic adenocarcinoma as well as highlights the potential of evaluating NP protein expression. PMID: 21448452 investigation of catalytic mechanisms involved in catalysis by PNP: transition states in arsenolysis and phosphorolysis PMID: 21348499 Results show that some regions, responsible for entrance and exit of substrate, present a conformational variability, which is dissected by dynamics simulation analysis. PMID: 19932753 PNP operating at maximum catalytic potential permits more rapid peptide amide deuterium exchange and greater conformational flexibility of water-peptide bond exchange rate than in either of the complexes with transition state analogues. PMID: 20108972 The optimum pH for PNP from human erythrocytes with xanthosine and xanthine is in the range 5-6, whereas those with guanosine, guanine, inosine & hypoxanthine are in the range 7-8. Possible PNP binding modes of Xan and Xao by mammalian PNPs are proposed. PMID: 12180982 Crystal structure of human purine nucleoside phosphorylase. PMID: 12914785 These data provide a framework in which to conduct genetic association studies of these two genes in relevant populations, thereby allowing hNP and hGSTO1-1 to be evaluated as potential susceptibility genes in human arsenicism. PMID: 12928150 investigation of the quaternary structure of recombinant human purine nucleoside phosphorylase PMID: 13679062 crystal structures in complex with inosine and 2',3'-dideoxyinosine, refined to 2.8A resolution using synchrotron radiation. The structures provide explanation for ligand binding, refine the purine-binding site and can be used for future inhibitor design. PMID: 14706628 several recurring mutations were found in PNP in patients with purine nucleoside phosphorylase deficiency by DNA sequence analysis PMID: 15571269 crystal structure of human PNP in complex with hypoxanthine, refined to 2.6A resoluti PMID: 15582582 findings suggest that the G51S PNP polymorphism is associated with a faster rate of cognitive decline in Alzheimer's disease patients, highlighting the important role of purine metabolism in the progression of this neurodegenerative disorder PMID: 17221831 Role of ionization of the phosphate cosubstrate on phosphorolysis by purine nucleoside phosphorylase PMID: 17639373 Altered thermodynamics from remote mutations altering human toward bovine purine nucleoside phosphorylase. PMID: 18281956 New interactions caused by the mutations increase the catalytic efficiency of the enzyme for formation of a late transition state with increased participation of the phosphate nucleophile. PMID: 18281957 Structural studies on NP are reported with a view towards a new specific scoring function. PMID: 18790691 Protein dynamics on the femtosecond to picosecond timescale are linked to enzymatic function. PMID: 18946041 Comparative analysis of the model of BfPNP and the structure of HsPNP allowed identification of structural features responsible for differences in the computationally determined ligand affinities PMID: 19172318 Results describe a tryptophan-free mutant of purine nucleoside phosphorylase and its dynamic activity. PMID: 19191546 Altered enthalpy-entropy compensation in picomolar transition state analogues of human purine nucleoside phosphorylase PMID: 19425594

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.